VKTHD_DENAN
ID VKTHD_DENAN Reviewed; 57 AA.
AC P00982;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 25-MAY-2022, entry version 97.
DE RecName: Full=Kunitz-type serine protease inhibitor homolog delta-dendrotoxin;
DE Short=Delta-DTX;
DE AltName: Full=Dendrotoxin delta-DaTX;
DE AltName: Full=Protease inhibitor K;
DE AltName: Full=Toxin C13S1C3;
DE AltName: Full=Venom basic protease inhibitor K;
OS Dendroaspis angusticeps (Eastern green mamba) (Naja angusticeps).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Elapidae; Elapinae; Dendroaspis.
OX NCBI_TaxID=8618;
RN [1]
RP PROTEIN SEQUENCE.
RX PubMed=7429422; DOI=10.1515/bchm2.1980.361.1.661;
RA Joubert F.J., Taljaard N.;
RT "Snake venoms. The amino acid sequences of two proteinase inhibitor
RT homologues from Dendroaspis angusticeps venom.";
RL Hoppe-Seyler's Z. Physiol. Chem. 361:661-674(1980).
RN [2]
RP PROTEIN SEQUENCE.
RX PubMed=2457792;
RA Benishin C.G., Sorensen R.G., Brown W.E., Krueger B.K., Blaustein M.P.;
RT "Four polypeptide components of green mamba venom selectively block certain
RT potassium channels in rat brain synaptosomes.";
RL Mol. Pharmacol. 34:152-159(1988).
RN [3]
RP FUNCTION, MUTAGENESIS OF ALA-1; LYS-3; TYR-4; LYS-6; LEU-7; PRO-8; VAL-9;
RP ARG-10; TYR-11; PRO-13; LYS-15; LYS-16; LYS-17; LYS-24; TRP-25; LYS-26;
RP LYS-28; LEU-31; ASP-34; ASN-41; ALA-42; ARG-44; LYS-46; GLU-49; GLU-50;
RP ARG-52; ARG-53 AND THR-54, AND SITE LYS-3; TYR-4; LYS-6; LEU-7; PRO-8;
RP ARG-10 AND LYS-26.
RX PubMed=10698633; DOI=10.1006/jmbi.2000.3522;
RA Imredy J.P., MacKinnon R.;
RT "Energetic and structural interactions between delta-dendrotoxin and a
RT voltage-gated potassium channel.";
RL J. Mol. Biol. 296:1283-1294(2000).
CC -!- FUNCTION: Serine protease inhibitor homolog that blocks voltage-gated
CC potassium channels (Kv). {ECO:0000269|PubMed:10698633}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- TOXIC DOSE: LD(50) is 15 mg/kg by intravenous injection.
CC -!- SIMILARITY: Belongs to the venom Kunitz-type family. {ECO:0000305}.
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DR PIR; A91691; TIEPVA.
DR AlphaFoldDB; P00982; -.
DR SMR; P00982; -.
DR MEROPS; I02.056; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0015459; F:potassium channel regulator activity; IEA:UniProtKB-KW.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:InterPro.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR CDD; cd00109; KU; 1.
DR Gene3D; 4.10.410.10; -; 1.
DR InterPro; IPR002223; Kunitz_BPTI.
DR InterPro; IPR036880; Kunitz_BPTI_sf.
DR InterPro; IPR020901; Prtase_inh_Kunz-CS.
DR Pfam; PF00014; Kunitz_BPTI; 1.
DR PRINTS; PR00759; BASICPTASE.
DR SMART; SM00131; KU; 1.
DR SUPFAM; SSF57362; SSF57362; 1.
DR PROSITE; PS00280; BPTI_KUNITZ_1; 1.
DR PROSITE; PS50279; BPTI_KUNITZ_2; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Ion channel impairing toxin;
KW Neurotoxin; Potassium channel impairing toxin; Secreted; Toxin;
KW Voltage-gated potassium channel impairing toxin.
FT CHAIN 1..57
FT /note="Kunitz-type serine protease inhibitor homolog delta-
FT dendrotoxin"
FT /id="PRO_0000155432"
FT DOMAIN 5..55
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT SITE 3
FT /note="Important for binding to potassium channels"
FT SITE 4
FT /note="Important for binding to potassium channels"
FT SITE 6
FT /note="Important for binding to potassium channels"
FT SITE 7
FT /note="May be important for binding to potassium channels"
FT SITE 8
FT /note="Important for binding to potassium channels"
FT SITE 10
FT /note="Important for binding to potassium channels"
FT SITE 26
FT /note="Important for binding to potassium channels"
FT DISULFID 5..55
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT DISULFID 14..38
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT DISULFID 30..51
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT MUTAGEN 1
FT /note="A->Q: Decrease in binding affinity for Kv."
FT /evidence="ECO:0000269|PubMed:10698633"
FT MUTAGEN 3
FT /note="K->A: Important decrease in binding affinity for
FT Kv.so."
FT /evidence="ECO:0000269|PubMed:10698633"
FT MUTAGEN 4
FT /note="Y->A: Important decrease in binding affinity for
FT Kv."
FT /evidence="ECO:0000269|PubMed:10698633"
FT MUTAGEN 6
FT /note="K->A: Important decrease in binding affinity for
FT Kv."
FT /evidence="ECO:0000269|PubMed:10698633"
FT MUTAGEN 7
FT /note="L->A: No change in binding affinity for Kv."
FT /evidence="ECO:0000269|PubMed:10698633"
FT MUTAGEN 8
FT /note="P->A: Important decrease in binding affinity for
FT Kv."
FT /evidence="ECO:0000269|PubMed:10698633"
FT MUTAGEN 9
FT /note="V->A: Slight increase in binding affinity for Kv."
FT /evidence="ECO:0000269|PubMed:10698633"
FT MUTAGEN 10
FT /note="R->A: Important decrease in binding affinity for
FT Kv."
FT /evidence="ECO:0000269|PubMed:10698633"
FT MUTAGEN 11
FT /note="Y->A: No change in binding affinity for Kv."
FT /evidence="ECO:0000269|PubMed:10698633"
FT MUTAGEN 13
FT /note="P->A: Slight decrease in binding affinity for Kv."
FT /evidence="ECO:0000269|PubMed:10698633"
FT MUTAGEN 15
FT /note="K->A: Slight decrease in binding affinity for Kv."
FT /evidence="ECO:0000269|PubMed:10698633"
FT MUTAGEN 16
FT /note="K->A: Increase in binding affinity for Kv."
FT /evidence="ECO:0000269|PubMed:10698633"
FT MUTAGEN 17
FT /note="K->A: No change in binding affinity for Kv."
FT /evidence="ECO:0000269|PubMed:10698633"
FT MUTAGEN 24
FT /note="K->A: Decrease in binding affinity for Kv."
FT /evidence="ECO:0000269|PubMed:10698633"
FT MUTAGEN 25
FT /note="W->A: Decrease in binding affinity for Kv."
FT /evidence="ECO:0000269|PubMed:10698633"
FT MUTAGEN 26
FT /note="K->A: Important decrease in binding affinity for
FT Kv."
FT /evidence="ECO:0000269|PubMed:10698633"
FT MUTAGEN 28
FT /note="K->A: Decrease in binding affinity for Kv."
FT /evidence="ECO:0000269|PubMed:10698633"
FT MUTAGEN 31
FT /note="L->A: Slight decrease in binding affinity for Kv."
FT /evidence="ECO:0000269|PubMed:10698633"
FT MUTAGEN 34
FT /note="D->A: Slight increase in binding affinity for Kv."
FT /evidence="ECO:0000269|PubMed:10698633"
FT MUTAGEN 41
FT /note="N->A: No change in binding affinity for Kv."
FT /evidence="ECO:0000269|PubMed:10698633"
FT MUTAGEN 42
FT /note="A->Q: Decrease in binding affinity for Kv."
FT /evidence="ECO:0000269|PubMed:10698633"
FT MUTAGEN 44
FT /note="R->A: Important decrease in binding affinity for
FT Kv."
FT /evidence="ECO:0000269|PubMed:10698633"
FT MUTAGEN 46
FT /note="K->A: Decrease in binding affinity for Kv."
FT /evidence="ECO:0000269|PubMed:10698633"
FT MUTAGEN 49
FT /note="E->A: No change in binding affinity for Kv."
FT /evidence="ECO:0000269|PubMed:10698633"
FT MUTAGEN 50
FT /note="E->A: Increase in binding affinity for Kv."
FT /evidence="ECO:0000269|PubMed:10698633"
FT MUTAGEN 52
FT /note="R->A: Slight decrease in binding affinity for Kv."
FT /evidence="ECO:0000269|PubMed:10698633"
FT MUTAGEN 53
FT /note="R->A: Decrease in binding affinity for Kv."
FT /evidence="ECO:0000269|PubMed:10698633"
FT MUTAGEN 54
FT /note="T->A: Decrease in binding affinity for Kv."
FT /evidence="ECO:0000269|PubMed:10698633"
SQ SEQUENCE 57 AA; 6574 MW; A4070CBBB141DE93 CRC64;
AAKYCKLPVR YGPCKKKIPS FYYKWKAKQC LPFDYSGCGG NANRFKTIEE CRRTCVG
